Roles of Various Cullin-RING E3 Ligases Involved in Hormonal and Stress Responses in Plants
2012
Seo, K.I., Yale University, New Haven, Connecticut, USA | Song, E.Y., Pusan National University, Busan, Republic of Korea | Chung, S.L., Yonsei University, Seoul, Republic of Korea | Lee, J.H., Pusan National University, Busan, Republic of Korea
Post-translational modification plays an important role in the regulation of protein stability, enzyme activity, and the cellular localization of proteins. Ubiquitination is a representative post-translational modification in eukaryotes that is mainly responsible for protein degradation. There have been a number of reports on the role of ubiquitination in various cellular responses in plants, such as regulation of the cell division cycle, stress responses and hormonal signaling. Among the three types of ubiquitination-related enzymes, E3 ubiquitin ligase is critical in determining substrate specificity. The importance of cullin-RING E3 ligase (CRL), a type of E3 ligase, has been emphasized during the recent decade due to its large number and its involvement in various plant cellular processes. Here, we describe how CRL E3 ligase complexes are involved in cellular events mediated by plant hormones and during plant stress adaptation while focusing on their substrate receptors.
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